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Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 16053

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16053
MolProbity Validation Chart

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Title: Attachment of an NMR-invisible solubility enhancement tag (INSET) using a sortase-mediated protein ligation method   PubMed: 19140010

Deposition date: 2008-12-07 Original release date: 2009-03-20

Authors: Kumeta, Hiroyuki; Kobashigawa, Yoshinori; Ogura, Kenji; Inagaki, Fuyuhiko

Citation: Kobashigawa, Yoshinori; Kumeta, Hiroyuki; Ogura, Kenji; Inagaki, Fuyuhiko. "Attachment of an NMR-invisible solubility enhancement tag (INSET) using a sortase-mediated protein ligation method"  J. Biomol. NMR 43, 145-150 (2009).

Assembly members:
entity, polymer, 141 residues, 8004.950 Da.

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
entity: GPGTFGTAKARYDFCARDRS ELSLKEGDIIKILNKKGQQG WWRGEIYGRIGWFPSNYVEE DYSEYLPETGGGSGSSMEYK LILNGKTLKGETTTEAVDAA TAEKVFKQYANDGVDGEWTY DDATKTFTVTEHSLEHHHHH H

Data sets:
Data typeCount
13C chemical shifts305
15N chemical shifts74
1H chemical shifts483

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 141 residues - 8004.950 Da.

1   GLYPROGLYTHRPHEGLYTHRALALYSALA
2   ARGTYRASPPHECYSALAARGASPARGSER
3   GLULEUSERLEULYSGLUGLYASPILEILE
4   LYSILELEUASNLYSLYSGLYGLNGLNGLY
5   TRPTRPARGGLYGLUILETYRGLYARGILE
6   GLYTRPPHEPROSERASNTYRVALGLUGLU
7   ASPTYRSERGLUTYRLEUPROGLUTHRGLY
8   GLYGLYSERGLYSERSERMETGLUTYRLYS
9   LEUILELEUASNGLYLYSTHRLEULYSGLY
10   GLUTHRTHRTHRGLUALAVALASPALAALA
11   THRALAGLULYSVALPHELYSGLNTYRALA
12   ASNASPGLYVALASPGLYGLUTRPTHRTYR
13   ASPASPALATHRLYSTHRPHETHRVALTHR
14   GLUHISSERLEUGLUHISHISHISHISHIS
15   HIS

Samples:

CN_label: entity, [U-13C; U-15N], ; MES 20 mM; DTT 2 mM; NaCl 150 mM

sample_conditions_1: ionic strength: 150 mM; pH: 7.0; pressure: 1.0 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCCN_labelisotropicsample_conditions_1
2D 1H-13C HSQCCN_labelisotropicsample_conditions_1
3D HNCOCN_labelisotropicsample_conditions_1
3D HN(CO)CACN_labelisotropicsample_conditions_1
3D HNCACN_labelisotropicsample_conditions_1
3D HN(CA)HACN_labelisotropicsample_conditions_1
3D CBCA(CO)NHCN_labelisotropicsample_conditions_1
3D HNCACBCN_labelisotropicsample_conditions_1
3D HCCH-TOCSYCN_labelisotropicsample_conditions_1
2D 1H-13C HSQC (Arom)CN_labelisotropicsample_conditions_1
2D (Hb)Cb(CgCd)HdCN_labelisotropicsample_conditions_1
2D (Hb)Cb(CgCdCe)HeCN_labelisotropicsample_conditions_1
3D HCCH-TOCSY (Arom)CN_labelisotropicsample_conditions_1
3D 1H-15N NOESYCN_labelisotropicsample_conditions_1
3D 1H-13C NOESYCN_labelisotropicsample_conditions_1
3D 1H-13C NOESY (Arom)CN_labelisotropicsample_conditions_1

Software:

NMRPipe v2.4, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

VNMR v6.1C, Varian - collection

RNMRTK v3, Alan Stern, Jeff Hoch - processing

SPARKY v3.110, Goddard - chemical shift assignment, peak picking, refinement

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Varian Unity 800 MHz
  • Varian Unity 600 MHz

Related Database Links:

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Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
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